UniProt ID | COPA_YEAST | |
---|---|---|
UniProt AC | P53622 | |
Protein Name | Coatomer subunit alpha | |
Gene Name | COP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 1201 | |
Subcellular Localization |
Cytoplasm. Golgi apparatus membrane Peripheral membrane protein Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. The coatomer is cytoplasmic or polymerized on the cytoplasmic side o |
|
Protein Description | The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.. | |
Protein Sequence | MKMLTKFESKSTRAKGIAFHPSRPWVLVALFSSTIQLWDYRMGTLLHRFEDHEGPVRGLDFHPTQPIFVSAGDDYTIKVWSLDTNKCLYTLTGHLDYVRTVFFHRELPWIISASDDQTIRIWNWQNRKEIACLTGHNHFVMCAQFHPTDDLIVSASLDETIRIWDISGLRKRHSAPGTSSFEEQMSAQQNLLDGSLGDCVVKFILEGHTRGVNWASFHPTLPLIVSGSDDRQVKLWRMSATKAWEVDTCRGHTNNVDSVIFHPHQNLIISVGEDKTLRVWDLDKRTPVKQFKRENDRFWLIAAHPHINLFGAAHDSGIMVFKLDRERPCSFIHQNQLFFVNAEKQIQSFNFQKRVASLPYASLKGIGQPWDAFRSISYNPSQHSVLVNEANGKFALVILPKQPVGAVEPTSVTQDTGNFATFVGRNRFVVYNKNTESVEVRSLENKVTRNIKVEETVRTIVAAGPGSVLVIHPREVILYDVQQGKKVSQLAVKNVKYVSWSLDGQYVALMSKHTITLATKKLELINSMHETIRIKSAAWDETGVLIYSTLNHIRYSLLNGDRGIIKTLEKTLYITKVQGKLVYCLNREGEIEILTIDPTEYRFKKALVNKNFPEVLRLIKDSNLVGQNIISYLQKSGYPEIALQFVQDPHIRFDLALEYGNLDVALDEAKKLNDSSTWERLIQEALAQGNASLAEMIYQTQHSFDKLSFLYLVTGDVNKLSKMQNIAQTREDFGSMLLNTFYNNSTKERSSIFAEGGSLPLAYAVAKANGDEAAASAFLEQAEVDEQDVTLPDQMDASNFVQRPVISKPLEKWPLKEAELSYFEKAVLGQIDDLTIDDETPAVNTTQEQEEPLGEENFNDEDIGEDEGAWDLGDEDLDVGEELPEEVEQGEITSPAQEVETAIWIKNSKLPAVLVAAGAFDAAVQALSKQVGVVKLEPLKKYFTNIYEGCRTYIPSTPCELPAQLGYVRAYDDTVSEDQILPYVPGLDVVNEKMNEGYKNFKLNKPDIAIECFREAIYRITLLMVDDAEDEKLAHKILETAREYILGLSIELERRSLKEGNTVRMLELAAYFTKAKLSPIHRTNALQVAMSQHFKHKNFLQASYFAGEFLKIISSGPRAEQARKIKNKADSMASDAIPIDFDPYAKFDICAATYKPIYEDTPSVSDPLTGSKYVITEKDKIDRIAMISKIGAPASGLRIRV | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
5 | Phosphorylation | ---MKMLTKFESKST ---CCCCCCCCCCCC | 30.13 | 28889911 | |
6 | Ubiquitination | --MKMLTKFESKSTR --CCCCCCCCCCCCC | 43.08 | 23749301 | |
9 | Phosphorylation | KMLTKFESKSTRAKG CCCCCCCCCCCCCCC | 34.73 | 30377154 | |
174 | Phosphorylation | SGLRKRHSAPGTSSF CCCCCCCCCCCCCCH | 39.94 | 30377154 | |
178 | Phosphorylation | KRHSAPGTSSFEEQM CCCCCCCCCCHHHHH | 21.82 | 30377154 | |
179 | Phosphorylation | RHSAPGTSSFEEQMS CCCCCCCCCHHHHHH | 38.66 | 30377154 | |
180 | Phosphorylation | HSAPGTSSFEEQMSA CCCCCCCCHHHHHHH | 36.19 | 28889911 | |
186 | Phosphorylation | SSFEEQMSAQQNLLD CCHHHHHHHHHCHHC | 23.71 | 19779198 | |
202 | Ubiquitination | SLGDCVVKFILEGHT CHHHHHHHHHHCCCC | 13.29 | 17644757 | |
242 | Ubiquitination | LWRMSATKAWEVDTC EEEEECCCCEEEECC | 51.74 | 23749301 | |
275 | Ubiquitination | IISVGEDKTLRVWDL EEEECCCCEEEEEEC | 45.19 | 23749301 | |
284 | Acetylation | LRVWDLDKRTPVKQF EEEEECCCCCCHHHC | 66.52 | 24489116 | |
286 | Phosphorylation | VWDLDKRTPVKQFKR EEECCCCCCHHHCCC | 37.87 | 21440633 | |
344 | Ubiquitination | LFFVNAEKQIQSFNF EEEECHHHHHHHCCH | 50.74 | 17644757 | |
353 | Acetylation | IQSFNFQKRVASLPY HHHCCHHHHHHCCCH | 44.71 | 24489116 | |
353 | Ubiquitination | IQSFNFQKRVASLPY HHHCCHHHHHHCCCH | 44.71 | 23749301 | |
364 | Ubiquitination | SLPYASLKGIGQPWD CCCHHHCCCCCCCHH | 46.09 | 23749301 | |
375 | Phosphorylation | QPWDAFRSISYNPSQ CCHHHHHHEECCCCC | 14.94 | 23607784 | |
377 | Phosphorylation | WDAFRSISYNPSQHS HHHHHHEECCCCCCE | 21.80 | 23607784 | |
378 | Phosphorylation | DAFRSISYNPSQHSV HHHHHEECCCCCCEE | 29.44 | 23607784 | |
381 | Phosphorylation | RSISYNPSQHSVLVN HHEECCCCCCEEEEE | 36.57 | 23607784 | |
384 | Phosphorylation | SYNPSQHSVLVNEAN ECCCCCCEEEEECCC | 14.98 | 23607784 | |
393 | Ubiquitination | LVNEANGKFALVILP EEECCCCEEEEEEEE | 27.54 | 17644757 | |
401 | Ubiquitination | FALVILPKQPVGAVE EEEEEEECCCCCEEC | 64.88 | 17644757 | |
433 | Ubiquitination | NRFVVYNKNTESVEV CEEEEEECCCCCEEE | 47.78 | 24961812 | |
433 | Acetylation | NRFVVYNKNTESVEV CEEEEEECCCCCEEE | 47.78 | 24489116 | |
446 | Ubiquitination | EVRSLENKVTRNIKV EEEECCCCHHCCCCH | 35.29 | 23749301 | |
452 | 2-Hydroxyisobutyrylation | NKVTRNIKVEETVRT CCHHCCCCHHHHHHH | 47.33 | - | |
485 | Succinylation | LYDVQQGKKVSQLAV EEEHHCCCEEEEEEE | 45.74 | 23954790 | |
497 | Phosphorylation | LAVKNVKYVSWSLDG EEECCCEEEEEEECH | 8.74 | 27017623 | |
506 | Phosphorylation | SWSLDGQYVALMSKH EEEECHHHEEEEECE | 8.01 | 27017623 | |
511 | Phosphorylation | GQYVALMSKHTITLA HHHEEEEECEEEEEH | 23.33 | 27017623 | |
535 | Ubiquitination | MHETIRIKSAAWDET HHCEEECCCCEECCC | 24.97 | 17644757 | |
570 | Acetylation | GIIKTLEKTLYITKV CHHHHHHHEEEEEEE | 47.12 | 24489116 | |
571 | Phosphorylation | IIKTLEKTLYITKVQ HHHHHHHEEEEEEEC | 18.54 | 21440633 | |
575 | Phosphorylation | LEKTLYITKVQGKLV HHHEEEEEEECCEEE | 16.17 | 21440633 | |
580 | Acetylation | YITKVQGKLVYCLNR EEEEECCEEEEECCC | 20.07 | 24489116 | |
610 | Acetylation | FKKALVNKNFPEVLR HHHHHCCCCCHHHHH | 53.11 | 22865919 | |
620 | Ubiquitination | PEVLRLIKDSNLVGQ HHHHHHHHCCCCCCH | 60.75 | 24961812 | |
635 | Ubiquitination | NIISYLQKSGYPEIA HHHHHHHHCCCCHHH | 43.16 | 17644757 | |
671 | Ubiquitination | VALDEAKKLNDSSTW HHHHHHHHCCCCHHH | 60.62 | 23749301 | |
722 | Ubiquitination | GDVNKLSKMQNIAQT CCHHHHHHCHHHHHH | 55.74 | 23749301 | |
750 | Phosphorylation | NNSTKERSSIFAEGG CCCCCCCCCCCCCCC | 28.95 | 21440633 | |
751 | Phosphorylation | NSTKERSSIFAEGGS CCCCCCCCCCCCCCC | 28.13 | 21440633 | |
812 | Acetylation | VISKPLEKWPLKEAE CCCCCHHHCCCCHHH | 62.89 | 22865919 | |
816 | Acetylation | PLEKWPLKEAELSYF CHHHCCCCHHHHHHH | 51.29 | 24489116 | |
906 | Ubiquitination | VETAIWIKNSKLPAV EEEEEEECCCCCCHH | 39.92 | 17644757 | |
909 | Ubiquitination | AIWIKNSKLPAVLVA EEEECCCCCCHHHHH | 68.81 | 17644757 | |
929 | Ubiquitination | AAVQALSKQVGVVKL HHHHHHHHCCCEEEC | 50.26 | 17644757 | |
956 | Phosphorylation | GCRTYIPSTPCELPA HHCCCCCCCCCCCCC | 35.11 | 28889911 | |
957 | Phosphorylation | CRTYIPSTPCELPAQ HCCCCCCCCCCCCCC | 26.97 | 28889911 | |
971 | Phosphorylation | QLGYVRAYDDTVSED CCCCEEECCCCCCHH | 12.09 | 27017623 | |
974 | Phosphorylation | YVRAYDDTVSEDQIL CEEECCCCCCHHHCC | 24.04 | 27017623 | |
976 | Phosphorylation | RAYDDTVSEDQILPY EECCCCCCHHHCCCC | 37.23 | 27017623 | |
993 | Ubiquitination | GLDVVNEKMNEGYKN CCHHHCHHCCHHHCC | 41.65 | 17644757 | |
1002 | Acetylation | NEGYKNFKLNKPDIA CHHHCCCCCCCCCHH | 61.62 | 24489116 | |
1032 | Acetylation | VDDAEDEKLAHKILE ECCCCCHHHHHHHHH | 64.39 | 24489116 | |
1056 | Phosphorylation | SIELERRSLKEGNTV CCEEHHHCCCCCCCE | 50.44 | 19823750 | |
1095 | Acetylation | VAMSQHFKHKNFLQA HHHHHHHCCCCHHHH | 52.09 | 24489116 | |
1097 | Ubiquitination | MSQHFKHKNFLQASY HHHHHCCCCHHHHHH | 50.41 | 17644757 | |
1111 | Ubiquitination | YFAGEFLKIISSGPR HHHHHHHHHHHCCHH | 43.23 | 17644757 | |
1172 | Ubiquitination | SDPLTGSKYVITEKD CCCCCCCCEEEECCC | 44.90 | 24961812 | |
1178 | Acetylation | SKYVITEKDKIDRIA CCEEEECCCHHCCEE | 56.52 | 24489116 | |
1189 | Ubiquitination | DRIAMISKIGAPASG CCEEEHHHCCCCCCC | 33.95 | 23749301 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
Oops, there are no upstream regulatory protein records of COPA_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of COPA_YEAST !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of COPA_YEAST !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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Phosphorylation | |
Reference | PubMed |
"A multidimensional chromatography technology for in-depthphosphoproteome analysis."; Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.; Mol. Cell. Proteomics 7:1389-1396(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-956 ANDTHR-957, AND MASS SPECTROMETRY. |